ID A0A1Q2GZF6_9GAMM Unreviewed; 311 AA.
AC A0A1Q2GZF6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN ORFNames=B0W48_12115 {ECO:0000313|EMBL:AQQ00477.1};
OS Pseudoalteromonas aliena.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=247523 {ECO:0000313|EMBL:AQQ00477.1, ECO:0000313|Proteomes:UP000188243};
RN [1] {ECO:0000313|EMBL:AQQ00477.1, ECO:0000313|Proteomes:UP000188243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EH1 {ECO:0000313|EMBL:AQQ00477.1,
RC ECO:0000313|Proteomes:UP000188243};
RA Kim E., Heo E., Kim H., Kim D.;
RT "Complete genome sequence of the cold-active Pseudoalteromonas aliena
RT strain EH1 isolated from Arctic seawater.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC Evidence={ECO:0000256|ARBA:ARBA00000677,
CC ECO:0000256|RuleBase:RU003993};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362042}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362042}.
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DR EMBL; CP019628; AQQ00477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2GZF6; -.
DR STRING; 247523.B0W48_12115; -.
DR KEGG; paln:B0W48_12115; -.
DR Proteomes; UP000188243; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.170.230.10; -; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR019766; Sign_pep_all-beta_subdom.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003993};
KW Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 61..282
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 91
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 311 AA; 35356 MW; A51FEF5560E7C47A CRC64;
MAGYFSVLLV LLTLGSGLIW LIDHLMFAPK RQARLAIAQT SAGAPLDEET AALIAPEPVI
TETAKSIFPM IAAITIFRSF IFEPFQIPSG SMMPTLLVGD FILVQKYSYG IKDPVWRTQL
VEMDEPERGD IVVFKYPLDD KVDYIKRTIG LPGDKVVYRD KRLYIQPNCN EGEIRKGELL
CNEFNKIDFK LINDDEFKQG PMPLARVSEN LTTVTHDILI NPQTPERKGR YYQQPGTPAD
EWVVPADHYF MMGDNRDNSQ DGRFWGFVPK ENLVGKAVFI WMSFEFENGP DDILPGWVPT
GVRFERLGNI Q
//